By 2030, one in five Americans will be a senior citizen. Worldwide, the number of people over 60 will triple by 2050 to nearly 2 billion, according to the Population Division of the United Nations.

What does that mean for scientists? Now more than ever they are devoted to studying the effects of aging and disease that hardly seemed relevant 100 years ago, when the life expectancy in the U.S. was about 47 years, according to the Centers for Disease Control and Prevention.

And they are producing amazing insights into the mysteries of why we age, grow frail, or contract age-related diseases.

Consider protein folding, one of the most essential, and poorly understood, processes of human life. When Wilfredo Freddie Colón, assistant professor of chemistry at Rensselaer, began his work on protein folding as a graduate student just over a decade ago, the relationship between protein folding and age-related diseases such as Alzheimers, Parkinsons, and Huntingtons was not established. Now researchers believe that understanding protein folding is at the heart of advances toward finding the causes and even cures for these usually fatal diseases.

[Un]folding the Mysteries of Proteins

Colón explains that proteins, which are made of a chain of linked amino acids, can only function if they fold into unique 3-D structures. No one knows how the string of amino acids folds. If we did, we would be able to manipulate proteins and design them to carry out certain functions, he says.

Colóns efforts to understand protein folding are widely recognized. Last year he received two prestigious awards from the National Science Foundation: the Faculty Early Career Development (CAREER) Award and the Presidential Early Career Award. Yet he remains humble, predicting that it will be at least 15 years before the mysteries of protein folding might be solved.

The process is complicated and long, explains Colón. He and his team study proteins in vitro, away from outside influences, which provides information on the protein itself but may lack important details on how it folds in its natural environment. He hopes someday to conduct in vivo studies through cell cultures, neuron cultures, and perhaps mice models, to address protein folding and misfolding as it occurs naturally.

What does this mean for the fight against Alzheimers, a common disease associated with aging? Alzheimers is an amyloid disease, a class of disease whose main characteristic is the formation of protein fibrils, or plaques, caused by protein buildup, or aggregation. Protein aggregation is a direct result of a protein misfolding, although not all protein misfolding leads to aggregation. In the case of Alzheimers, fibrils form in the brain, which leads to deterioration of brain tissue.

There are about 20 known syndromes or diseases in the amyloid family, including Huntingtons disease, mad cow disease, and Type II diabetes. If we can understand how any one protein can form amyloid fibrils, then we may be able to apply that understanding to all proteins, explains Colón, who studies a protein not connected to Alzheimers but to a more rare amyloid disease.

The mechanism by which proteins form fibrils is not well understood in any situation, and researchers do not even know whether it is the fibrils or the process of forming fibrils that is toxic to the body. If, as Colón suspects, something in the process is the culprit, then drugs to target the destruction of the fibrils may not have the desired results.

With many questions still unanswered, Colón remains optimistic. If researchers can map the human genome, perhaps we can figure out how proteins fold, he says.

Colón is not the only Rensselaer researcher making a mark on the myriad issues faced by the aging population. Rensselaer is committed to research in the biosciences and biotechnology that has a tremendous impact on health care issues affecting the world. From aging eyes to brittle bones to better cartilage, researchers at Rensselaer are working to make aging an easier, healthier, although still inevitable, process.